Sharon Sweitzer

TL;DR: SIRT1 can be directly activated through an allosteric mechanism common to chemically diverse STACs, and specific hydrophobic motifs found in SIRT1 substrates such as PGC-1α and FOXO3a facilitate Sirtuin-activating compounds (STACs) activation by STacs.

TL;DR: Yuan et al. as mentioned in this paper found that specific hydrophobic motifs found in SIRT1 substrates such as PGC-1α and FOXO3a facilitate SIRT 1 activation by STACs.

TL;DR: It is demonstrated that small molecule activators of SIRT1 (STACs) enhance deacetylation of cellular p65 protein, which results in the suppression of TNF α-induced NF-κB transcriptional activation and reduction of LPS-stimulated TNFα secretion in a SIRT 1-dependent manner.

TL;DR: The identification and characterization of a novel cytokine-like gene family using structure-based methods to search for novel four-helix-bundle cytokines in genomics databases is reported, and it is found that FAM3A and FAM3B protein were both localized to the islets of Langerhans of the endocrine pancreas.

TL;DR: The design and characterization of an engineered human SIRT1 construct containing the minimal structural elements required for lysine deacetylation and catalytic activation by small molecule sirtuin-activating compounds (STACs) are reported and the STAC-binding site within the N-terminal domain of hSIRT1 is revealed.